[HTML][HTML] Src family kinases phosphorylate protein kinase C δ on tyrosine residues and modify the neoplastic phenotype of skin keratinocytes
E Joseloff, C Cataisson, H Aamodt, H Ocheni… - Journal of Biological …, 2002 - ASBMB
Protein kinase C δ (PKC δ) is tyrosine-phosphorylated and catalytically inactive in mouse
keratinocytes transformed by a ras oncogene. In several other model systems, Src kinases
are upstream regulators of PKC δ. To examine this relationship in epidermal carcinogenesis,
v-ras transformed mouse keratinocytes were treated with a selective Src kinase inhibitor (PD
173958). PD 173958 decreased autophosphorylation of Src, Fyn, and Lyn kinases and
prevented tyrosine phosphorylation of the Src kinase substrate p120. PD 173958 also …
keratinocytes transformed by a ras oncogene. In several other model systems, Src kinases
are upstream regulators of PKC δ. To examine this relationship in epidermal carcinogenesis,
v-ras transformed mouse keratinocytes were treated with a selective Src kinase inhibitor (PD
173958). PD 173958 decreased autophosphorylation of Src, Fyn, and Lyn kinases and
prevented tyrosine phosphorylation of the Src kinase substrate p120. PD 173958 also …
